Structural And Functional Properties Of Batx, A New Lys49 Phospholipase A2 Homologue Isolated From The Venom Of The Snake Bothrops Alternatus

dc.creatorPonce-Soto L.A.
dc.creatorLomonte B.
dc.creatorGutierrez J.M.
dc.creatorRodrigues-Simioni L.
dc.creatorNovello J.C.
dc.creatorMarangoni S.
dc.date2007
dc.date2015-06-30T18:47:03Z
dc.date2015-11-26T14:35:23Z
dc.date2015-06-30T18:47:03Z
dc.date2015-11-26T14:35:23Z
dc.date.accessioned2018-03-28T21:38:48Z
dc.date.available2018-03-28T21:38:48Z
dc.identifier
dc.identifierBiochimica Et Biophysica Acta - General Subjects. , v. 1770, n. 4, p. 585 - 593, 2007.
dc.identifier3044165
dc.identifier10.1016/j.bbagen.2006.11.015
dc.identifierhttp://www.scopus.com/inward/record.url?eid=2-s2.0-33847152992&partnerID=40&md5=ffc9058e0f5dbca54847c86e5882369c
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/104760
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/104760
dc.identifier2-s2.0-33847152992
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1248359
dc.descriptionBaTX PLA2, a K49 phospholipase A2 homologue was purified from Bothrops alternatus venom after two chromatographic steps, molecular exclusion on Superdex 75 and reverse phase HPLC on μ-Bondapack C-18. A molecular mass of 13898.71 Da was determined by MALDI-TOF mass spectrometry. The amino acid composition showed that BaTX has a high content of Lys, Tyr, Gly, Pro, and 14 half-Cys residues, typical of a basic PLA2. The complete amino acid sequence of BaTX PLA2 contains 121 residues, resulting in a calculated pI value of 8.63. This sequence shows high identity values when compared to other K49 PLA2s isolated from the venoms of viperid snakes. Lower identity is observed in comparison to D49 PLA2s. The sequence was SLFELGKMIL QETGKNPAKS YGAYYCYCGW GGQGQPKDAT DRCCYVHKCC YKKLTGCNPK KDRYSYSWKD KTIVCGENNS CLKELCECDK AVAICLRENL NTYNKKYRYY LKPLCKKADA C. In mice, BaTX induced myonecrosis and edema, upon intramuscular or subcutaneous injections, respectively. The LD50 of BaTX was 7 μg/g body weight, by intravenous route. In vitro, the toxin caused a potent blockade of neuromuscular transmission in young chicken biventer cervicis preparations. The blockage 50% was achieved at a concentration of 0.03 μM: 40 ± 0.4 min and 0.07 μM: 35 ± 0.3 min. Moreover, this protein induced a rapid cytolytic effect upon mouse skeletal muscle myoblasts in culture. Thus, the combined structural and functional information obtained identify BaTX as a new member of the K49 PLA2 family, which presents the typical bioactivities described for such proteins. © 2006 Elsevier B.V. All rights reserved.
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dc.languageen
dc.publisher
dc.relationBiochimica et Biophysica Acta - General Subjects
dc.rightsfechado
dc.sourceScopus
dc.titleStructural And Functional Properties Of Batx, A New Lys49 Phospholipase A2 Homologue Isolated From The Venom Of The Snake Bothrops Alternatus
dc.typeArtículos de revistas


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